UniProtKB - P23528 (COF1_HUMAN)
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- BLAST>sp|P23528|COF1_HUMAN Cofilin-1 OS=Homo sapiens OX=9606 GN=CFL1 PE=1 SV=3 MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDV GQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASS KDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL
- Align
Cofilin-1
CFL1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
4 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"Determining the differences in actin binding by human ADF and cofilin."
Yeoh S., Pope B., Mannherz H.G., Weeds A.
J. Mol. Biol. 315:911-925(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.15"Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics."
Gohla A., Birkenfeld J., Bokoch G.M.
Nat. Cell Biol. 7:21-29(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, DEPHOSPHORYLATION BY PDXP. - Ref.24"Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.30"Beta-arrestin-dependent activation of the cofilin pathway is required for the scavenging activity of the atypical chemokine receptor D6."
Borroni E.M., Cancellieri C., Vacchini A., Benureau Y., Lagane B., Bachelerie F., Arenzana-Seisdedos F., Mizuno K., Mantovani A., Bonecchi R., Locati M.
Sci. Signal. 6:RA30-RA30(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- actin filament binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- signaling receptor binding Source: Ensembl
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- actin cytoskeleton organization Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- actin filament depolymerization Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- actin filament fragmentation Source: Ensembl
- cytoskeleton organization Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- establishment of cell polarity Source: Ensembl
- interleukin-12-mediated signaling pathway Source: Reactome
- mitotic cytokinesis Source: Ensembl
- negative regulation of apoptotic process Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- neural crest cell migration Source: Ensembl
- neural fold formation Source: Ensembl
- positive regulation by host of viral process Source: AgBase <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of actin filament depolymerization Source: Ensembl
- protein phosphorylation Source: Ensembl
- regulation of cell morphogenesis Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of dendritic spine morphogenesis Source: ParkinsonsUK-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- response to amino acid Source: Ensembl
- response to virus Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- Rho protein signal transduction Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Actin-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-114608 Platelet degranulation R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation R-HSA-3928662 EPHB-mediated forward signaling R-HSA-399954 Sema3A PAK dependent Axon repulsion R-HSA-5627117 RHO GTPases Activate ROCKs R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P23528 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P23528 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Cofilin-1Alternative name(s): 18 kDa phosphoprotein Short name: p18 Cofilin, non-muscle isoform |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:CFL1 Synonyms:CFL |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000172757.12 |
Human Gene Nomenclature Database More...HGNCi | HGNC:1874 CFL1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 601442 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P23528 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Plasma membrane
- ruffle membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics."
Gohla A., Birkenfeld J., Bokoch G.M.
Nat. Cell Biol. 7:21-29(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, DEPHOSPHORYLATION BY PDXP.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics."
Gohla A., Birkenfeld J., Bokoch G.M.
Nat. Cell Biol. 7:21-29(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, DEPHOSPHORYLATION BY PDXP.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics."
Gohla A., Birkenfeld J., Bokoch G.M.
Nat. Cell Biol. 7:21-29(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, DEPHOSPHORYLATION BY PDXP.
- lamellipodium membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics."
Gohla A., Birkenfeld J., Bokoch G.M.
Nat. Cell Biol. 7:21-29(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, DEPHOSPHORYLATION BY PDXP.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics."
Gohla A., Birkenfeld J., Bokoch G.M.
Nat. Cell Biol. 7:21-29(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, DEPHOSPHORYLATION BY PDXP.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics."
Gohla A., Birkenfeld J., Bokoch G.M.
Nat. Cell Biol. 7:21-29(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, DEPHOSPHORYLATION BY PDXP.
- ruffle membrane 1 Publication
Cytoskeleton
- cytoskeleton 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics."
Gohla A., Birkenfeld J., Bokoch G.M.
Nat. Cell Biol. 7:21-29(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, DEPHOSPHORYLATION BY PDXP.
- cytoskeleton 1 Publication
Nucleus
- Nucleus matrix 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics."
Gohla A., Birkenfeld J., Bokoch G.M.
Nat. Cell Biol. 7:21-29(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, DEPHOSPHORYLATION BY PDXP.
- Nucleus matrix 1 Publication
Other locations
- lamellipodium By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
Note: Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide.- lamellipodium By similarity
Cytoskeleton
- cortical actin cytoskeleton Source: Ensembl
Cytosol
- cytosol Source: Reactome
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- extracellular space Source: UniProtKBInferred from high throughput direct assayi
Nucleus
- nuclear matrix Source: UniProtKB-SubCell
- nucleus Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
Plasma Membrane
- lamellipodium membrane Source: UniProtKB-SubCell
- ruffle membrane Source: UniProtKB-SubCell
Other locations
- cell-cell junction Source: Ensembl
- cytoplasm Source: AgBase <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- focal adhesion Source: UniProtKBInferred from high throughput direct assayi
- lamellipodium Source: UniProtKB
- membrane Source: UniProtKBInferred from high throughput direct assayi
- vesicle Source: UniProtKBInferred from high throughput direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Organism-specific databases
DisGeNET More...DisGeNETi | 1072 |
Open Targets More...OpenTargetsi | ENSG00000172757 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA26423 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1075129 |
Drug and drug target database More...DrugBanki | DB04147 Lauryl Dimethylamine-N-Oxide |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | CFL1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 116848 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000214898 | 2 – 166 | Cofilin-1Add BLAST | 165 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylalanineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 3 | Phosphoserine; by NRKCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 8 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 13 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 25 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 41 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 68 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 73 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 132 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 140 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 144 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 156 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.13"Cofilin phosphorylation and actin polymerization by NRK/NESK, a member of the germinal center kinase family."
Nakano K., Kanai-Azuma M., Kanai Y., Moriyama K., Yazaki K., Hayashi Y., Kitamura N.
Exp. Cell Res. 287:219-227(2003) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-3 BY NRK. - Ref.30"Beta-arrestin-dependent activation of the cofilin pathway is required for the scavenging activity of the atypical chemokine receptor D6."
Borroni E.M., Cancellieri C., Vacchini A., Benureau Y., Lagane B., Bachelerie F., Arenzana-Seisdedos F., Mizuno K., Mantovani A., Bonecchi R., Locati M.
Sci. Signal. 6:RA30-RA30(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P23528 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P23528 |
PeptideAtlas More...PeptideAtlasi | P23528 |
PRoteomics IDEntifications database More...PRIDEi | P23528 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54128 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P23528 |
2D gel databases
DOSAC-COBS 2D-PAGE database More...DOSAC-COBS-2DPAGEi | P23528 |
USC-OGP 2-DE database More...OGPi | P23528 |
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00012011 |
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P23528 |
University College Dublin 2-DE Proteome Database More...UCD-2DPAGEi | P23528 |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | P23528 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P23528 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P23528 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P23528 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | P23528 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
Leong W.F., Chow V.T.
Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000172757 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P23528 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P23528 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB033687 CAB037077 HPA053761 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ACTB | P60709 | 6 | EBI-352733,EBI-353944 | |
| ACTG1 | P63261 | 8 | EBI-352733,EBI-351292 | |
| ATXN1 | P54253 | 5 | EBI-352733,EBI-930964 | |
| CFL2 | Q549N0 | 3 | EBI-352733,EBI-10201319 | |
| HUNK | P57058 | 2 | EBI-352733,EBI-3959804 | |
| LIMK1 | P53667 | 3 | EBI-352733,EBI-444403 | |
| M | P0DOE7 | 2 | EBI-352733,EBI-10042882 | From Human respiratory syncytial virus A (strain A2). |
| PLD1 | Q13393 | 4 | EBI-352733,EBI-2827556 | |
| PLD2 | O14939 | 2 | EBI-352733,EBI-1053996 | |
| PS1TP5BP1 | Q1KLZ0 | 3 | EBI-352733,EBI-9978131 | |
| SSH1 | Q8WYL5 | 2 | EBI-352733,EBI-1222387 | |
| YWHAG | P61981 | 2 | EBI-352733,EBI-359832 | |
| YWHAZ | P63104 | 3 | EBI-352733,EBI-347088 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- actin filament binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- signaling receptor binding Source: Ensembl
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 107499, 155 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P23528 |
Database of interacting proteins More...DIPi | DIP-33000N |
Protein interaction database and analysis system More...IntActi | P23528, 84 interactors |
Molecular INTeraction database More...MINTi | P23528 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000309629 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 9 – 19 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 26 – 31 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 33 – 40 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 44 – 56 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 57 – 59 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 61 – 63 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 67 – 74 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 77 – 79 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 81 – 90 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 95 – 104 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 111 – 127 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 134 – 139 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 140 – 144 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 147 – 154 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 155 – 157 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 160 – 165 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P23528 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P23528 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P23528 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 4 – 153 | ADF-HPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 150 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 30 – 34 | Nuclear localization signalSequence analysis | 5 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1735 Eukaryota ENOG41122P5 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00440000033289 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000039697 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000381 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P23528 |
KEGG Orthology (KO) More...KOi | K05765 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P23528 |
TreeFam database of animal gene trees More...TreeFami | TF328601 |
Family and domain databases
Conserved Domains Database More...CDDi | cd11286 ADF_cofilin_like, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.20.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002108 ADF-H IPR029006 ADF-H/Gelsolin-like_dom_sf IPR017904 ADF/Cofilin IPR027234 Cofilin_1 |
The PANTHER Classification System More...PANTHERi | PTHR11913 PTHR11913, 1 hit PTHR11913:SF17 PTHR11913:SF17, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00241 Cofilin_ADF, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00006 COFILIN |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00102 ADF, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51263 ADF_H, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE
60 70 80 90 100
EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV
110 120 130 140 150
FIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA
160
EKLGGSAVIS LEGKPL
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | D00682 mRNA Translation: BAA00589.1 U21909 mRNA Translation: AAA64501.1 X95404 mRNA Translation: CAA64685.1 BT006846 mRNA Translation: AAP35492.1 AK097690 mRNA Translation: BAG53513.1 CH471076 Genomic DNA Translation: EAW74449.1 BC011005 mRNA Translation: AAH11005.1 BC012265 mRNA Translation: AAH12265.1 BC012318 mRNA Translation: AAH12318.1 BC018256 mRNA Translation: AAH18256.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS8114.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S12632 |
NCBI Reference Sequences More...RefSeqi | NP_005498.1, NM_005507.2 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.170622 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000308162; ENSP00000309629; ENSG00000172757 ENST00000525451; ENSP00000432660; ENSG00000172757 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 1072 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:1072 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P23528 | Cofilin 1 (Non-muscle), isoform CRA_b | 166 | |||
| CFL1 isoform 3 | 166 | ||||
| Cofilin-1 | 166 | ||||
| CFL1 isoform 4 | 166 | ||||
| Uncharacterized protein | 166 | ||||
| +18 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P23528 | Cofilin-1 | 166 | |||
| cofilin-1 | 166 | ||||
| Cofilin-1 | 166 | ||||
| Uncharacterized protein | 166 | ||||
| UPI0004401CE2 | 243 | ||||
| +33 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Wikipedia Cofilin entry |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | D00682 mRNA Translation: BAA00589.1 U21909 mRNA Translation: AAA64501.1 X95404 mRNA Translation: CAA64685.1 BT006846 mRNA Translation: AAP35492.1 AK097690 mRNA Translation: BAG53513.1 CH471076 Genomic DNA Translation: EAW74449.1 BC011005 mRNA Translation: AAH11005.1 BC012265 mRNA Translation: AAH12265.1 BC012318 mRNA Translation: AAH12318.1 BC018256 mRNA Translation: AAH18256.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS8114.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S12632 |
NCBI Reference Sequences More...RefSeqi | NP_005498.1, NM_005507.2 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.170622 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1Q8G | NMR | - | A | 1-166 | [»] | |
| 1Q8X | NMR | - | A | 1-166 | [»] | |
| 3J0S | electron microscopy | 9.00 | M/N/O/P/Q/R/S/T/U/V/W/X | 1-166 | [»] | |
| 4BEX | X-ray | 2.80 | 1 | 1-166 | [»] | |
| 5HVK | X-ray | 3.50 | B/D | 2-166 | [»] | |
| 5L6W | X-ray | 2.53 | C | 1-166 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P23528 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P23528 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 107499, 155 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P23528 |
Database of interacting proteins More...DIPi | DIP-33000N |
Protein interaction database and analysis system More...IntActi | P23528, 84 interactors |
Molecular INTeraction database More...MINTi | P23528 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000309629 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1075129 |
Drug and drug target database More...DrugBanki | DB04147 Lauryl Dimethylamine-N-Oxide |
PTM databases
CarbonylDB database of protein carbonylation sites More...CarbonylDBi | P23528 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P23528 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P23528 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P23528 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | CFL1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 116848 |
2D gel databases
DOSAC-COBS 2D-PAGE database More...DOSAC-COBS-2DPAGEi | P23528 |
USC-OGP 2-DE database More...OGPi | P23528 |
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00012011 |
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P23528 |
University College Dublin 2-DE Proteome Database More...UCD-2DPAGEi | P23528 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P23528 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P23528 |
PeptideAtlas More...PeptideAtlasi | P23528 |
PRoteomics IDEntifications database More...PRIDEi | P23528 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54128 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P23528 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 1072 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000308162; ENSP00000309629; ENSG00000172757 ENST00000525451; ENSP00000432660; ENSG00000172757 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 1072 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:1072 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 1072 |
DisGeNET More...DisGeNETi | 1072 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000172757.12 |
GeneCards: human genes, protein and diseases More...GeneCardsi | CFL1 |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0009009 |
Human Gene Nomenclature Database More...HGNCi | HGNC:1874 CFL1 |
Human Protein Atlas More...HPAi | CAB033687 CAB037077 HPA053761 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 601442 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P23528 |
Open Targets More...OpenTargetsi | ENSG00000172757 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA26423 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1735 Eukaryota ENOG41122P5 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00440000033289 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000039697 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000381 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P23528 |
KEGG Orthology (KO) More...KOi | K05765 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P23528 |
TreeFam database of animal gene trees More...TreeFami | TF328601 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-114608 Platelet degranulation R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation R-HSA-3928662 EPHB-mediated forward signaling R-HSA-399954 Sema3A PAK dependent Axon repulsion R-HSA-5627117 RHO GTPases Activate ROCKs R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P23528 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P23528 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | CFL1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P23528 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Cofilin_1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 1072 |
CutDB - Proteolytic event database More...PMAP-CutDBi | P23528 |
Protein Ontology More...PROi | PR:P23528 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000172757 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P23528 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P23528 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd11286 ADF_cofilin_like, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.20.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002108 ADF-H IPR029006 ADF-H/Gelsolin-like_dom_sf IPR017904 ADF/Cofilin IPR027234 Cofilin_1 |
The PANTHER Classification System More...PANTHERi | PTHR11913 PTHR11913, 1 hit PTHR11913:SF17 PTHR11913:SF17, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00241 Cofilin_ADF, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00006 COFILIN |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00102 ADF, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51263 ADF_H, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | COF1_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P23528Primary (citable) accession number: P23528 Secondary accession number(s): B3KUQ1, Q53Y87, Q9UCA2 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1991 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | July 18, 2018 | |
| This is version 210 of the entry and version 3 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
